LACCASE35 enhances lignification and resistance against <i>Pseudomonas syringae</i> pv. <i>actinidiae</i> infection in kiwifruit
Yawei Li, Dongle Zhang, Xiaojie Wang, Fuxi Bai, Rui Li, Rongrong Zhou, Sifan Wu, Zemin Fang, Wei Liu, Lili Huang, Pu Liu
Abstract
Kiwifruit bacterial canker, a highly destructive disease caused by Pseudomonas syringae pv. actinidiae (Psa), seriously affects kiwifruit (Actinidia spp.) production. Lignin deposition in infected cells serves as a defense mechanism, effectively suppressing pathogen growth. However, the underlying process remains unclear. In this study, we determined that Psa infection leads to a significant increase in S-lignin accumulation in kiwifruit. The S/G ratio in lignin was higher in a Psa-resistant cultivar than in a Psa-sensitive cultivar. Furthermore, kiwifruit laccase 35 (AcLac35), encoding an enzyme in the lignin biosynthesis pathway with characteristic laccase activity, showed tissue-specific expression in plants and was upregulated following infection by Psa. Overexpressing AcLac35 in kiwifruit leaves resulted in greater lignin content than in wild-type leaves, leading to the formation of thicker cell walls, and also activated plant-pathogen interactions and MAPK pathways, thereby enhancing resistance against Psa infection. Yeast 1-hybrid assays, dual-LUC reporter assays, electrophoretic mobility shift assays, and transient injection experiments indicated that SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE 9 (AcSPL9) can bind to the AcLac35 promoter, thereby positively regulating its expression. Moreover, overexpression of AcSPL9 increased lignin accumulation in kiwifruit leaves, enhancing resistance to Psa, while virus-induced gene silencing of AcSPL9 expression reduced this resistance. Our findings reveal the function of AsSPL9-AcLac35 in kiwifruit, providing insight into enhancing resistance against Psa in kiwifruit.